Reviewed, UniProtKB/Swiss-Prot P38207 (APN2_YEAST)

Names and origin

Protein names

Recommended name:
    DNA-(apurinic or apyrimidinic site) lyase 2
    EC=4.2.99.18
Alternative name(s):
    AP endonuclease 2
    Apurinic-apyrimidinic endonuclease 2

Gene names

Name:	APN2
Synonyms:	ETH1
Ordered Locus Names:	YBL019W
ORF Names:	YBL0443

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA.
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Subcellular location	Nucleus.
Miscellaneous	Present with 414 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the DNA repair enzymes AP/exoA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	base-excision repair Ref.2 Inferred from genetic interaction. Source: SGD
Cellular component	nucleus Ref.3 Inferred by curator. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-(apurinic or apyrimidinic site) lyase activity Ref.3 Inferred from direct assay. Source: SGD double-stranded DNA specific 3'-5' exodeoxyribonuclease activity Inferred from direct assay. Source: SGD endonuclease activity Inferred from electronic annotation. Source: InterPro phosphoric diester hydrolase activity Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	DNA-(apurinic or apyrimidinic site) lyase 2		PRO_0000200020

Sequences

	Sequence		Length	Mass (Da)
	P38207-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: E3947C4D904C53FB	FASTA	520	59,445
	10 20 30 40 50 60 MSSSENTLLD GKSENTIRFL TFNVNGIRTF FHYQPFSQMN QSLRSVFDFF RADIITFQEL 70 80 90 100 110 120 KTEKLSISKW GRVDGFYSFI SIPQTRKGYS GVGCWIRIPE KNHPLYHALQ VVKAEEGITG 130 140 150 160 170 180 YLTIKNGKHS AISYRNDVNQ GIGGYDSLDP DLDEKSALEL DSEGRCVMVE LACGIVIISV 190 200 210 220 230 240 YCPANSNSSE EGEMFRLRFL KVLLRRVRNL DKIGKKIVLM GDVNVCRDLI DSADTLEQFS 250 260 270 280 290 300 IPITDPMGGT KLEAQYRDKA IQFIINPDTP HRRIFNQILA DSLLPDASKR GILIDTTRLI 310 320 330 340 350 360 QTRNRLKMYT VWNMLKNLRP SNYGSRIDFI LVSLKLERCI KAADILPDIL GSDHCPVYSD 370 380 390 400 410 420 LDILDDRIEP GTTQVPIPKF EARYKYNLRN HNVLEMFAKK DTNKESNKQK YCVSKVMNTK 430 440 450 460 470 480 KNSNIKNKSL DSFFQKVNGE KDDRIKESSE IPQQAKKRIS TPKLNFKDVF GKPPLCRHGE 490 500 510 520 ESMLKTSKTS ANPGRKFWIC KRSRGDSNNT ESSCGFFQWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites." Johnson R.E., Torres-Ramos C.A., Izumi T., Mitra S., Prakash S., Prakash L. Genes Dev. 12:3137-3143(1998) [PubMed: 9765213] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Apurinic endonuclease activity of yeast Apn2 protein." Unk I., Haracska L., Johnson R.E., Prakash S., Prakash L. J. Biol. Chem. 275:22427-22434(2000) [PubMed: 10806210] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z35780 Genomic DNA. Translation: CAA84838.1.
PIR	S45753.
RefSeq	NP_009534.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3930N.
IntAct	P38207. 4 interactions.
STRING	P38207.
Genome annotation databases
Ensembl	YBL019W; YBL019W; YBL019W; Saccharomyces cerevisiae. [Genome view]
GeneID	852262.
KEGG	sce:YBL019W.
NMPDR	fig|4932.3.peg.227.
Organism-specific databases
CYGD	YBL019w.
SGD	S000000115. APN2.
Phylogenomic databases
HOGENOM	P38207.
OMA	MYTVWNT
OrthoDB	EOG91RRBK
Enzyme and pathway databases
BRENDA	4.2.99.18. 250.
Gene expression databases
ArrayExpress	P38207.
Genevestigator	P38207.
GermOnline	YBL019W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR020848. AP_endonuclease_F1_CS. IPR005135. Endo/exonuclease/phosphatase. IPR004808. exoDNase_III. IPR010666. Znf_GRF. [Graphical view]
PANTHER	PTHR22748. ExoIII_xth. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. PF06839. zf-GRF. 1 hit. [Graphical view]
PROSITE	PS00726. AP_NUCLEASE_F1_1. False negative. PS00727. AP_NUCLEASE_F1_2. False negative. PS00728. AP_NUCLEASE_F1_3. 1 hit. PS51435. AP_NUCLEASE_F1_4. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	970856.

Entry information

Entry name

APN2_YEAST

Accession

Primary (citable) accession number: P38207

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 24, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)